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| | <StructureSection load='3n1k' size='340' side='right'caption='[[3n1k]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3n1k' size='340' side='right'caption='[[3n1k]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3n1k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Potato Potato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3N1K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3n1k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_tuberosum Solanum tuberosum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N1K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N1K FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3n1h|3n1h]], [[3n1i|3n1i]], [[3n1j|3n1j]], [[3n1l|3n1l]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.702Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">StWhy2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4113 Potato])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3n1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1k OCA], [https://pdbe.org/3n1k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n1k RCSB], [https://www.ebi.ac.uk/pdbsum/3n1k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n1k ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3n1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n1k OCA], [http://pdbe.org/3n1k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3n1k RCSB], [http://www.ebi.ac.uk/pdbsum/3n1k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3n1k ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/WHY2_SOLTU WHY2_SOLTU] Single-stranded DNA-binding protein that may be involved in the maintenance of mitochondrial genome stability by preventing break-induced DNA rearrangements.<ref>PMID:21911368</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Potato]] | + | [[Category: Solanum tuberosum]] |
| - | [[Category: Brisson, N]] | + | [[Category: Brisson N]] |
| - | [[Category: Cappadocia, L]] | + | [[Category: Cappadocia L]] |
| - | [[Category: Sygusch, J]] | + | [[Category: Sygusch J]] |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Plant]]
| + | |
| - | [[Category: Protein-dna complex]]
| + | |
| - | [[Category: Single-stranded dna binding protein]]
| + | |
| - | [[Category: Whirly]]
| + | |
| Structural highlights
Function
WHY2_SOLTU Single-stranded DNA-binding protein that may be involved in the maintenance of mitochondrial genome stability by preventing break-induced DNA rearrangements.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
DNA double-strand breaks are highly detrimental to all organisms and need to be quickly and accurately repaired. Although several proteins are known to maintain plastid and mitochondrial genome stability in plants, little is known about the mechanisms of DNA repair in these organelles and the roles of specific proteins. Here, using ciprofloxacin as a DNA damaging agent specific to the organelles, we show that plastids and mitochondria can repair DNA double-strand breaks through an error-prone pathway similar to the microhomology-mediated break-induced replication observed in humans, yeast, and bacteria. This pathway is negatively regulated by the single-stranded DNA (ssDNA) binding proteins from the Whirly family, thus indicating that these proteins could contribute to the accurate repair of plant organelle genomes. To understand the role of Whirly proteins in this process, we solved the crystal structures of several Whirly-DNA complexes. These reveal a nonsequence-specific ssDNA binding mechanism in which DNA is stabilized between domains of adjacent subunits and rendered unavailable for duplex formation and/or protein interactions. Our results suggest a model in which the binding of Whirly proteins to ssDNA would favor accurate repair of DNA double-strand breaks over an error-prone microhomology-mediated break-induced replication repair pathway.
Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair.,Cappadocia L, Marechal A, Parent JS, Lepage E, Sygusch J, Brisson N Plant Cell. 2010 Jun;22(6):1849-67. Epub 2010 Jun 15. PMID:20551348[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Cappadocia L, Parent JS, Zampini E, Lepage E, Sygusch J, Brisson N. A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage. Nucleic Acids Res. 2011 Sep 12. PMID:21911368 doi:10.1093/nar/gkr740
- ↑ Cappadocia L, Marechal A, Parent JS, Lepage E, Sygusch J, Brisson N. Crystal structures of DNA-Whirly complexes and their role in Arabidopsis organelle genome repair. Plant Cell. 2010 Jun;22(6):1849-67. Epub 2010 Jun 15. PMID:20551348 doi:10.1105/tpc.109.071399
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